CN104066447A - 重组蛋白及其治疗用途 - Google Patents

重组蛋白及其治疗用途 Download PDF

Info

Publication number: CN104066447A
Authority: CN; China
Prior art keywords: somatomedin; recombiant; sequence; proteins; recombiant protein
Prior art date: 2011-11-23
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Pending

Application number

CN201280067891.1A

Other languages

English (en)

Chinese (zh)

Inventor

基思·艾伦·查尔顿

E·德杭特

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

In3bio Ltd

Original Assignee

Bioven 3 Ltd

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2011-11-23

Filing date

2012-11-21

Publication date

2014-09-24

2012-11-21 Application filed by Bioven 3 Ltd filed Critical Bioven 3 Ltd

2012-11-21 Priority to CN201810569310.3A priority Critical patent/CN108864261A/zh

2012-11-21 Priority to CN201810569766.XA priority patent/CN108864291A/zh

2014-09-24 Publication of CN104066447A publication Critical patent/CN104066447A/zh

Status Pending legal-status Critical Current

Links

102000007056 Recombinant Fusion Proteins Human genes 0.000 title abstract description 21
108010008281 Recombinant Fusion Proteins Proteins 0.000 title abstract description 21
230000001225 therapeutic effect Effects 0.000 title description 4
239000000427 antigen Substances 0.000 claims abstract description 96
102000036639 antigens Human genes 0.000 claims abstract description 96
108091007433 antigens Proteins 0.000 claims abstract description 96
102000005962 receptors Human genes 0.000 claims abstract description 89
206010028980 Neoplasm Diseases 0.000 claims abstract description 88
230000002163 immunogen Effects 0.000 claims abstract description 23
108090000623 proteins and genes Proteins 0.000 claims description 319
102000004169 proteins and genes Human genes 0.000 claims description 313
108090000723 Insulin-Like Growth Factor I Proteins 0.000 claims description 144
102000013275 Somatomedins Human genes 0.000 claims description 133
VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 claims description 115
102000009024 Epidermal Growth Factor Human genes 0.000 claims description 101
101800003838 Epidermal growth factor Proteins 0.000 claims description 98
229940116977 epidermal growth factor Drugs 0.000 claims description 97
108010049048 Cholera Toxin Proteins 0.000 claims description 93
102000009016 Cholera Toxin Human genes 0.000 claims description 90
108090000765 processed proteins & peptides Proteins 0.000 claims description 64
238000000034 method Methods 0.000 claims description 42
102000004887 Transforming Growth Factor beta Human genes 0.000 claims description 19
108090001012 Transforming Growth Factor beta Proteins 0.000 claims description 19
ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 claims description 19
229920000642 polymer Polymers 0.000 claims description 16
239000000178 monomer Substances 0.000 claims description 14
125000006850 spacer group Chemical group 0.000 claims description 14
108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 claims description 13
102000009524 Vascular Endothelial Growth Factor A Human genes 0.000 claims description 13
238000002360 preparation method Methods 0.000 claims description 13
102000004218 Insulin-Like Growth Factor I Human genes 0.000 claims description 11
108010072866 Prostate-Specific Antigen Proteins 0.000 claims description 10
102100038358 Prostate-specific antigen Human genes 0.000 claims description 10
101150029707 ERBB2 gene Proteins 0.000 claims description 9
108010073923 Vascular Endothelial Growth Factor C Proteins 0.000 claims description 9
238000006386 neutralization reaction Methods 0.000 claims description 8
210000001744 T-lymphocyte Anatomy 0.000 claims description 7
108090000379 Fibroblast growth factor 2 Proteins 0.000 claims description 6
102000003974 Fibroblast growth factor 2 Human genes 0.000 claims description 6
108010019530 Vascular Endothelial Growth Factors Proteins 0.000 claims description 6
102000005789 Vascular Endothelial Growth Factors Human genes 0.000 claims description 6
108090001117 Insulin-Like Growth Factor II Proteins 0.000 claims description 5
102000048143 Insulin-Like Growth Factor II Human genes 0.000 claims description 5
229940031348 multivalent vaccine Drugs 0.000 claims description 5
102000016979 Other receptors Human genes 0.000 claims description 4
102000006747 Transforming Growth Factor alpha Human genes 0.000 claims description 4
101800004564 Transforming growth factor alpha Proteins 0.000 claims description 4
108010073925 Vascular Endothelial Growth Factor B Proteins 0.000 claims description 4
102100038217 Vascular endothelial growth factor B Human genes 0.000 claims description 4
238000002255 vaccination Methods 0.000 claims description 4
102000003971 Fibroblast Growth Factor 1 Human genes 0.000 claims 3
108090000386 Fibroblast Growth Factor 1 Proteins 0.000 claims 3
102000009520 Vascular Endothelial Growth Factor C Human genes 0.000 claims 3
102000056372 ErbB-3 Receptor Human genes 0.000 claims 2
102100030086 Receptor tyrosine-protein kinase erbB-2 Human genes 0.000 claims 2
108020003175 receptors Proteins 0.000 abstract description 72
239000003102 growth factor Substances 0.000 abstract description 11
108091026890 Coding region Proteins 0.000 abstract description 5
235000018102 proteins Nutrition 0.000 description 236
229960005486 vaccine Drugs 0.000 description 41
239000000203 mixture Substances 0.000 description 31
150000001413 amino acids Chemical class 0.000 description 29
241000699670 Mus sp. Species 0.000 description 28
235000001014 amino acid Nutrition 0.000 description 28
239000002671 adjuvant Substances 0.000 description 27
101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 20
101001055320 Myxine glutinosa Insulin-like growth factor Proteins 0.000 description 20
230000027455 binding Effects 0.000 description 20
238000000746 purification Methods 0.000 description 20
102100037852 Insulin-like growth factor I Human genes 0.000 description 19
238000002965 ELISA Methods 0.000 description 18
230000036039 immunity Effects 0.000 description 18
238000010790 dilution Methods 0.000 description 17
239000012895 dilution Substances 0.000 description 17
239000003795 chemical substances by application Substances 0.000 description 16
210000004027 cell Anatomy 0.000 description 15
238000012360 testing method Methods 0.000 description 15
229920001184 polypeptide Polymers 0.000 description 14
102000004196 processed proteins & peptides Human genes 0.000 description 14
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 13
230000004048 modification Effects 0.000 description 13
238000012986 modification Methods 0.000 description 13
239000008194 pharmaceutical composition Substances 0.000 description 13
230000004044 response Effects 0.000 description 13
238000002372 labelling Methods 0.000 description 12
239000001397 quillaja saponaria molina bark Substances 0.000 description 12
229930182490 saponin Natural products 0.000 description 12
150000007949 saponins Chemical class 0.000 description 12
210000002966 serum Anatomy 0.000 description 11
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 10
241000607626 Vibrio cholerae Species 0.000 description 9
230000005875 antibody response Effects 0.000 description 9
201000011510 cancer Diseases 0.000 description 9
201000010099 disease Diseases 0.000 description 9
230000005847 immunogenicity Effects 0.000 description 9
230000009182 swimming Effects 0.000 description 9
238000005406 washing Methods 0.000 description 9
208000017667 Chronic Disease Diseases 0.000 description 8
239000000872 buffer Substances 0.000 description 8
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 8
102000037865 fusion proteins Human genes 0.000 description 8
108020001507 fusion proteins Proteins 0.000 description 8
230000028993 immune response Effects 0.000 description 8
210000000987 immune system Anatomy 0.000 description 8
238000011081 inoculation Methods 0.000 description 8
230000003472 neutralizing effect Effects 0.000 description 8
239000002953 phosphate buffered saline Substances 0.000 description 8
239000000047 product Substances 0.000 description 8
206010009944 Colon cancer Diseases 0.000 description 7
241001465754 Metazoa Species 0.000 description 7
241000283973 Oryctolagus cuniculus Species 0.000 description 7
230000001804 emulsifying effect Effects 0.000 description 7
239000011780 sodium chloride Substances 0.000 description 7
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 7
CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 6
102000018233 Fibroblast Growth Factor Human genes 0.000 description 6
108050007372 Fibroblast Growth Factor Proteins 0.000 description 6
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
102100038232 Vascular endothelial growth factor C Human genes 0.000 description 6
238000004458 analytical method Methods 0.000 description 6
230000015572 biosynthetic process Effects 0.000 description 6
238000006243 chemical reaction Methods 0.000 description 6
239000003085 diluting agent Substances 0.000 description 6
PRAKJMSDJKAYCZ-UHFFFAOYSA-N dodecahydrosqualene Natural products CC(C)CCCC(C)CCCC(C)CCCCC(C)CCCC(C)CCCC(C)C PRAKJMSDJKAYCZ-UHFFFAOYSA-N 0.000 description 6
238000005516 engineering process Methods 0.000 description 6
229940126864 fibroblast growth factor Drugs 0.000 description 6
239000000568 immunological adjuvant Substances 0.000 description 6
230000003211 malignant effect Effects 0.000 description 6
238000004519 manufacturing process Methods 0.000 description 6
239000003607 modifier Substances 0.000 description 6
239000000546 pharmaceutical excipient Substances 0.000 description 6
230000008569 process Effects 0.000 description 6
UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 5
206010006187 Breast cancer Diseases 0.000 description 5
208000026310 Breast neoplasm Diseases 0.000 description 5
241000283707 Capra Species 0.000 description 5
102000014914 Carrier Proteins Human genes 0.000 description 5
108010078791 Carrier Proteins Proteins 0.000 description 5
-1 IGF-l Proteins 0.000 description 5
201000008275 breast carcinoma Diseases 0.000 description 5
239000003599 detergent Substances 0.000 description 5
239000000539 dimer Substances 0.000 description 5
238000001962 electrophoresis Methods 0.000 description 5
230000007613 environmental effect Effects 0.000 description 5
229930182830 galactose Natural products 0.000 description 5
239000001963 growth medium Substances 0.000 description 5
239000000463 material Substances 0.000 description 5
238000011160 research Methods 0.000 description 5
230000009870 specific binding Effects 0.000 description 5
239000000758 substrate Substances 0.000 description 5
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
206010005003 Bladder cancer Diseases 0.000 description 4
208000003174 Brain Neoplasms Diseases 0.000 description 4
102100021935 C-C motif chemokine 26 Human genes 0.000 description 4
108090000565 Capsid Proteins Proteins 0.000 description 4
208000017897 Carcinoma of esophagus Diseases 0.000 description 4
102100023321 Ceruloplasmin Human genes 0.000 description 4
108020004414 DNA Proteins 0.000 description 4
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
101150084418 EGF gene Proteins 0.000 description 4
102000009465 Growth Factor Receptors Human genes 0.000 description 4
108010009202 Growth Factor Receptors Proteins 0.000 description 4
101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 4
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 4
206010058467 Lung neoplasm malignant Diseases 0.000 description 4
206010030155 Oesophageal carcinoma Diseases 0.000 description 4
206010033128 Ovarian cancer Diseases 0.000 description 4
206010061535 Ovarian neoplasm Diseases 0.000 description 4
102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 4
108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 4
229930006000 Sucrose Natural products 0.000 description 4
208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 4
235000004279 alanine Nutrition 0.000 description 4
230000002421 anti-septic effect Effects 0.000 description 4
230000001580 bacterial effect Effects 0.000 description 4
230000008859 change Effects 0.000 description 4
238000012412 chemical coupling Methods 0.000 description 4
HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 4
208000029742 colonic neoplasm Diseases 0.000 description 4
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
235000018417 cysteine Nutrition 0.000 description 4
239000003814 drug Substances 0.000 description 4
201000005619 esophageal carcinoma Diseases 0.000 description 4
239000013604 expression vector Substances 0.000 description 4
238000001502 gel electrophoresis Methods 0.000 description 4
239000004519 grease Substances 0.000 description 4
230000012010 growth Effects 0.000 description 4
108020001756 ligand binding domains Proteins 0.000 description 4
239000007788 liquid Substances 0.000 description 4
239000006210 lotion Substances 0.000 description 4
238000006384 oligomerization reaction Methods 0.000 description 4
230000002829 reductive effect Effects 0.000 description 4
239000005720 sucrose Substances 0.000 description 4
238000003786 synthesis reaction Methods 0.000 description 4
230000002194 synthesizing effect Effects 0.000 description 4
239000013638 trimer Substances 0.000 description 4
201000005112 urinary bladder cancer Diseases 0.000 description 4
229920000936 Agarose Polymers 0.000 description 3
WVDDGKGOMKODPV-UHFFFAOYSA-N Benzyl alcohol Chemical compound OCC1=CC=CC=C1 WVDDGKGOMKODPV-UHFFFAOYSA-N 0.000 description 3
201000009030 Carcinoma Diseases 0.000 description 3
241000196324 Embryophyta Species 0.000 description 3
241000588724 Escherichia coli Species 0.000 description 3
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
108091008603 HGF receptors Proteins 0.000 description 3
102100022623 Hepatocyte growth factor receptor Human genes 0.000 description 3
102000013462 Interleukin-12 Human genes 0.000 description 3
108010065805 Interleukin-12 Proteins 0.000 description 3
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
108010054278 Lac Repressors Proteins 0.000 description 3
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
241000699666 Mus <mouse, genus> Species 0.000 description 3
DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
102000009661 Repressor Proteins Human genes 0.000 description 3
CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 3
108091005735 TGF-beta receptors Proteins 0.000 description 3
102000016715 Transforming Growth Factor beta Receptors Human genes 0.000 description 3
241000700605 Viruses Species 0.000 description 3
QNHQEUFMIKRNTB-UHFFFAOYSA-N aesculetin Natural products C1CC(=O)OC2=C1C=C(O)C(O)=C2 QNHQEUFMIKRNTB-UHFFFAOYSA-N 0.000 description 3
GUAFOGOEJLSQBT-UHFFFAOYSA-N aesculetin dimethyl ether Natural products C1=CC(=O)OC2=C1C=C(OC)C(OC)=C2 GUAFOGOEJLSQBT-UHFFFAOYSA-N 0.000 description 3
239000003963 antioxidant agent Substances 0.000 description 3
230000003078 antioxidant effect Effects 0.000 description 3
235000006708 antioxidants Nutrition 0.000 description 3
238000013459 approach Methods 0.000 description 3
239000011668 ascorbic acid Substances 0.000 description 3
235000010323 ascorbic acid Nutrition 0.000 description 3
229960005070 ascorbic acid Drugs 0.000 description 3
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 3
238000009835 boiling Methods 0.000 description 3
230000008878 coupling Effects 0.000 description 3
238000010168 coupling process Methods 0.000 description 3
238000005859 coupling reaction Methods 0.000 description 3
238000001514 detection method Methods 0.000 description 3
UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 3
239000003937 drug carrier Substances 0.000 description 3
230000000694 effects Effects 0.000 description 3
ILEDWLMCKZNDJK-UHFFFAOYSA-N esculetin Chemical compound C1=CC(=O)OC2=C1C=C(O)C(O)=C2 ILEDWLMCKZNDJK-UHFFFAOYSA-N 0.000 description 3
238000002474 experimental method Methods 0.000 description 3
239000008103 glucose Substances 0.000 description 3
230000002949 hemolytic effect Effects 0.000 description 3
235000010181 horse chestnut Nutrition 0.000 description 3
239000004615 ingredient Substances 0.000 description 3
230000003993 interaction Effects 0.000 description 3
230000000968 intestinal effect Effects 0.000 description 3
235000013336 milk Nutrition 0.000 description 3
239000008267 milk Substances 0.000 description 3
210000004080 milk Anatomy 0.000 description 3
208000002154 non-small cell lung carcinoma Diseases 0.000 description 3
230000003287 optical effect Effects 0.000 description 3
230000036961 partial effect Effects 0.000 description 3
230000000505 pernicious effect Effects 0.000 description 3
229920000136 polysorbate Polymers 0.000 description 3
239000000843 powder Substances 0.000 description 3
239000011347 resin Substances 0.000 description 3
229920005989 resin Polymers 0.000 description 3
238000000926 separation method Methods 0.000 description 3
239000000243 solution Substances 0.000 description 3
239000002904 solvent Substances 0.000 description 3
239000003381 stabilizer Substances 0.000 description 3
239000000725 suspension Substances 0.000 description 3
238000002560 therapeutic procedure Methods 0.000 description 3
231100000765 toxin Toxicity 0.000 description 3
239000003053 toxin Substances 0.000 description 3
208000029729 tumor suppressor gene on chromosome 11 Diseases 0.000 description 3
WQZGKKKJIJFFOK-SVZMEOIVSA-N (+)-Galactose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-SVZMEOIVSA-N 0.000 description 2
YYGNTYWPHWGJRM-UHFFFAOYSA-N (6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene Chemical compound CC(C)=CCCC(C)=CCCC(C)=CCCC=C(C)CCC=C(C)CCC=C(C)C YYGNTYWPHWGJRM-UHFFFAOYSA-N 0.000 description 2
241000157280 Aesculus hippocastanum Species 0.000 description 2
208000023275 Autoimmune disease Diseases 0.000 description 2
108090001008 Avidin Proteins 0.000 description 2
101710132601 Capsid protein Proteins 0.000 description 2
101710094648 Coat protein Proteins 0.000 description 2
208000001333 Colorectal Neoplasms Diseases 0.000 description 2
102000004127 Cytokines Human genes 0.000 description 2
108090000695 Cytokines Proteins 0.000 description 2
102000001301 EGF receptor Human genes 0.000 description 2
108060006698 EGF receptor Proteins 0.000 description 2
SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 2
108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 2
102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 2
101710186643 Insulin-2 Proteins 0.000 description 2
102100037850 Interferon gamma Human genes 0.000 description 2
108010074328 Interferon-gamma Proteins 0.000 description 2
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 2
241000186781 Listeria Species 0.000 description 2
101710125418 Major capsid protein Proteins 0.000 description 2
101100386050 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cys-14 gene Proteins 0.000 description 2
239000000020 Nitrocellulose Substances 0.000 description 2
101710141454 Nucleoprotein Proteins 0.000 description 2
241000288906 Primates Species 0.000 description 2
101710083689 Probable capsid protein Proteins 0.000 description 2
241000589516 Pseudomonas Species 0.000 description 2
101000679735 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 60S ribosomal protein L16-A Proteins 0.000 description 2
102000007562 Serum Albumin Human genes 0.000 description 2
108010071390 Serum Albumin Proteins 0.000 description 2
BHEOSNUKNHRBNM-UHFFFAOYSA-N Tetramethylsqualene Natural products CC(=C)C(C)CCC(=C)C(C)CCC(C)=CCCC=C(C)CCC(C)C(=C)CCC(C)C(C)=C BHEOSNUKNHRBNM-UHFFFAOYSA-N 0.000 description 2
102000046299 Transforming Growth Factor beta1 Human genes 0.000 description 2
102000009618 Transforming Growth Factors Human genes 0.000 description 2
108010009583 Transforming Growth Factors Proteins 0.000 description 2
101800002279 Transforming growth factor beta-1 Proteins 0.000 description 2
UZQJVUCHXGYFLQ-AYDHOLPZSA-N [(2s,3r,4s,5r,6r)-4-[(2s,3r,4s,5r,6r)-4-[(2r,3r,4s,5r,6r)-4-[(2s,3r,4s,5r,6r)-3,5-dihydroxy-6-(hydroxymethyl)-4-[(2s,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,5-dihydroxy-6-(hy Chemical compound O([C@H]1[C@H](O)[C@@H](CO)O[C@H]([C@@H]1O)O[C@H]1[C@H](O)[C@@H](CO)O[C@H]([C@@H]1O)O[C@H]1CC[C@]2(C)[C@H]3CC=C4[C@@]([C@@]3(CC[C@H]2[C@@]1(C=O)C)C)(C)CC(O)[C@]1(CCC(CC14)(C)C)C(=O)O[C@H]1[C@@H]([C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O[C@H]4[C@@H]([C@@H](O[C@H]5[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O5)O)[C@H](O)[C@@H](CO)O4)O)[C@H](O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO)O2)O)[C@H](O)[C@@H](CO)O1)O)[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O UZQJVUCHXGYFLQ-AYDHOLPZSA-N 0.000 description 2
239000000443 aerosol Substances 0.000 description 2
230000000259 anti-tumor effect Effects 0.000 description 2
238000003556 assay Methods 0.000 description 2
229920002988 biodegradable polymer Polymers 0.000 description 2
239000004621 biodegradable polymer Substances 0.000 description 2
229920001400 block copolymer Polymers 0.000 description 2
230000032823 cell division Effects 0.000 description 2
230000004663 cell proliferation Effects 0.000 description 2
235000012000 cholesterol Nutrition 0.000 description 2
239000011248 coating agent Substances 0.000 description 2
238000000576 coating method Methods 0.000 description 2
201000010989 colorectal carcinoma Diseases 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
230000007850 degeneration Effects 0.000 description 2
238000010586 diagram Methods 0.000 description 2
230000029087 digestion Effects 0.000 description 2
238000006471 dimerization reaction Methods 0.000 description 2
229960003983 diphtheria toxoid Drugs 0.000 description 2
229940079593 drug Drugs 0.000 description 2
239000000975 dye Substances 0.000 description 2
239000000839 emulsion Substances 0.000 description 2
210000002615 epidermis Anatomy 0.000 description 2
239000000796 flavoring agent Substances 0.000 description 2
235000013355 food flavoring agent Nutrition 0.000 description 2
239000012634 fragment Substances 0.000 description 2
230000005714 functional activity Effects 0.000 description 2
230000004927 fusion Effects 0.000 description 2
201000010536 head and neck cancer Diseases 0.000 description 2
208000014829 head and neck neoplasm Diseases 0.000 description 2
230000005745 host immune response Effects 0.000 description 2
239000002955 immunomodulating agent Substances 0.000 description 2
230000002584 immunomodulator Effects 0.000 description 2
229940121354 immunomodulator Drugs 0.000 description 2
230000003308 immunostimulating effect Effects 0.000 description 2
238000001727 in vivo Methods 0.000 description 2
238000002347 injection Methods 0.000 description 2
239000007924 injection Substances 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
238000007918 intramuscular administration Methods 0.000 description 2
238000001990 intravenous administration Methods 0.000 description 2
239000008101 lactose Substances 0.000 description 2
230000000670 limiting effect Effects 0.000 description 2
208000020816 lung neoplasm Diseases 0.000 description 2
HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
239000002609 medium Substances 0.000 description 2
239000002480 mineral oil Substances 0.000 description 2
229940042472 mineral oil Drugs 0.000 description 2
235000010446 mineral oil Nutrition 0.000 description 2
230000004899 motility Effects 0.000 description 2
201000006417 multiple sclerosis Diseases 0.000 description 2
JXTPJDDICSTXJX-UHFFFAOYSA-N n-Triacontane Natural products CCCCCCCCCCCCCCCCCCCCCCCCCCCCCC JXTPJDDICSTXJX-UHFFFAOYSA-N 0.000 description 2
230000007935 neutral effect Effects 0.000 description 2
229920001220 nitrocellulos Polymers 0.000 description 2
230000003204 osmotic effect Effects 0.000 description 2
230000037361 pathway Effects 0.000 description 2
210000001322 periplasm Anatomy 0.000 description 2
239000012071 phase Substances 0.000 description 2
201000001514 prostate carcinoma Diseases 0.000 description 2
238000012797 qualification Methods 0.000 description 2
230000009467 reduction Effects 0.000 description 2
230000001105 regulatory effect Effects 0.000 description 2
230000000717 retained effect Effects 0.000 description 2
238000007789 sealing Methods 0.000 description 2
238000004088 simulation Methods 0.000 description 2
GEHJYWRUCIMESM-UHFFFAOYSA-L sodium sulfite Chemical compound [Na+].[Na+].[O-]S([O-])=O GEHJYWRUCIMESM-UHFFFAOYSA-L 0.000 description 2
239000007787 solid Substances 0.000 description 2
239000007790 solid phase Substances 0.000 description 2
241000894007 species Species 0.000 description 2
229940032094 squalane Drugs 0.000 description 2
229940031439 squalene Drugs 0.000 description 2
TUHBEKDERLKLEC-UHFFFAOYSA-N squalene Natural products CC(=CCCC(=CCCC(=CCCC=C(/C)CCC=C(/C)CC=C(C)C)C)C)C TUHBEKDERLKLEC-UHFFFAOYSA-N 0.000 description 2
238000010561 standard procedure Methods 0.000 description 2
238000010254 subcutaneous injection Methods 0.000 description 2
239000007929 subcutaneous injection Substances 0.000 description 2
239000006228 supernatant Substances 0.000 description 2
239000004094 surface-active agent Substances 0.000 description 2
239000000375 suspending agent Substances 0.000 description 2
229960000814 tetanus toxoid Drugs 0.000 description 2
210000001519 tissue Anatomy 0.000 description 2
229940099456 transforming growth factor beta 1 Drugs 0.000 description 2
241000701161 unidentified adenovirus Species 0.000 description 2
241001515965 unidentified phage Species 0.000 description 2
201000011531 vascular cancer Diseases 0.000 description 2
239000013598 vector Substances 0.000 description 2
230000003612 virological effect Effects 0.000 description 2
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
238000001262 western blot Methods 0.000 description 2
FTLYMKDSHNWQKD-UHFFFAOYSA-N (2,4,5-trichlorophenyl)boronic acid Chemical compound OB(O)C1=CC(Cl)=C(Cl)C=C1Cl FTLYMKDSHNWQKD-UHFFFAOYSA-N 0.000 description 1
OOIBFPKQHULHSQ-UHFFFAOYSA-N (3-hydroxy-1-adamantyl) 2-methylprop-2-enoate Chemical compound C1C(C2)CC3CC2(O)CC1(OC(=O)C(=C)C)C3 OOIBFPKQHULHSQ-UHFFFAOYSA-N 0.000 description 1
MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 description 1
PXFBZOLANLWPMH-UHFFFAOYSA-N 16-Epiaffinine Natural products C1C(C2=CC=CC=C2N2)=C2C(=O)CC2C(=CC)CN(C)C1C2CO PXFBZOLANLWPMH-UHFFFAOYSA-N 0.000 description 1
JECYNCQXXKQDJN-UHFFFAOYSA-N 2-(2-methylhexan-2-yloxymethyl)oxirane Chemical compound CCCCC(C)(C)OCC1CO1 JECYNCQXXKQDJN-UHFFFAOYSA-N 0.000 description 1
YELMWJNXDALKFE-UHFFFAOYSA-N 3h-imidazo[4,5-f]quinoxaline Chemical compound N1=CC=NC2=C(NC=N3)C3=CC=C21 YELMWJNXDALKFE-UHFFFAOYSA-N 0.000 description 1
FJKROLUGYXJWQN-UHFFFAOYSA-M 4-hydroxybenzoate Chemical compound OC1=CC=C(C([O-])=O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-M 0.000 description 1
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
241000157282 Aesculus Species 0.000 description 1
241001119624 Aesculus chinensis Species 0.000 description 1
GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
239000005995 Aluminium silicate Substances 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
241000282836 Camelus dromedarius Species 0.000 description 1
241000589875 Campylobacter jejuni Species 0.000 description 1
229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
238000007445 Chromatographic isolation Methods 0.000 description 1
KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
229920000858 Cyclodextrin Polymers 0.000 description 1
FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
229920001353 Dextrin Polymers 0.000 description 1
239000004375 Dextrin Substances 0.000 description 1
240000003421 Dianthus chinensis Species 0.000 description 1
240000001879 Digitalis lutea Species 0.000 description 1
QRLVDLBMBULFAL-UHFFFAOYSA-N Digitonin Natural products CC1CCC2(OC1)OC3C(O)C4C5CCC6CC(OC7OC(CO)C(OC8OC(CO)C(O)C(OC9OCC(O)C(O)C9OC%10OC(CO)C(O)C(OC%11OC(CO)C(O)C(O)C%11O)C%10O)C8O)C(O)C7O)C(O)CC6(C)C5CCC4(C)C3C2C QRLVDLBMBULFAL-UHFFFAOYSA-N 0.000 description 1
102000018386 EGF Family of Proteins Human genes 0.000 description 1
108010066486 EGF Family of Proteins Proteins 0.000 description 1
101710146739 Enterotoxin Proteins 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
101000867232 Escherichia coli Heat-stable enterotoxin II Proteins 0.000 description 1
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
239000001856 Ethyl cellulose Substances 0.000 description 1
ZZSNKZQZMQGXPY-UHFFFAOYSA-N Ethyl cellulose Chemical compound CCOCC1OC(OC)C(OCC)C(OCC)C1OC1C(O)C(O)C(OC)C(CO)O1 ZZSNKZQZMQGXPY-UHFFFAOYSA-N 0.000 description 1
241000206602 Eukaryota Species 0.000 description 1
229920001503 Glucan Polymers 0.000 description 1
108010053070 Glutathione Disulfide Proteins 0.000 description 1
239000004471 Glycine Substances 0.000 description 1
241001316290 Gypsophila Species 0.000 description 1
108090000100 Hepatocyte Growth Factor Proteins 0.000 description 1
102100021866 Hepatocyte growth factor Human genes 0.000 description 1
101500025419 Homo sapiens Epidermal growth factor Proteins 0.000 description 1
101001076292 Homo sapiens Insulin-like growth factor II Proteins 0.000 description 1
108010001336 Horseradish Peroxidase Proteins 0.000 description 1
108090000144 Human Proteins Proteins 0.000 description 1
102000003839 Human Proteins Human genes 0.000 description 1
101150088952 IGF1 gene Proteins 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
244000283207 Indigofera tinctoria Species 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
102100025947 Insulin-like growth factor II Human genes 0.000 description 1
108010002350 Interleukin-2 Proteins 0.000 description 1
102000000588 Interleukin-2 Human genes 0.000 description 1
108010002586 Interleukin-7 Proteins 0.000 description 1
102000000704 Interleukin-7 Human genes 0.000 description 1
206010022998 Irritability Diseases 0.000 description 1
241000124008 Mammalia Species 0.000 description 1
229930195725 Mannitol Natural products 0.000 description 1
125000003047 N-acetyl group Chemical group 0.000 description 1
241001644525 Nastus productus Species 0.000 description 1
241000588650 Neisseria meningitidis Species 0.000 description 1
102000015336 Nerve Growth Factor Human genes 0.000 description 1
108010025020 Nerve Growth Factor Proteins 0.000 description 1
101100442582 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) spe-1 gene Proteins 0.000 description 1
241001597008 Nomeidae Species 0.000 description 1
108091028043 Nucleic acid sequence Proteins 0.000 description 1
240000007817 Olea europaea Species 0.000 description 1
101710116435 Outer membrane protein Proteins 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
108010081690 Pertussis Toxin Proteins 0.000 description 1
239000002202 Polyethylene glycol Substances 0.000 description 1
108010034634 Repressor Proteins Proteins 0.000 description 1
241000283984 Rodentia Species 0.000 description 1
241000219287 Saponaria Species 0.000 description 1
240000003946 Saponaria officinalis Species 0.000 description 1
102000009203 Sema domains Human genes 0.000 description 1
108050000099 Sema domains Proteins 0.000 description 1
YMTLKLXDFCSCNX-BYPYZUCNSA-N Ser-Gly-Gly Chemical compound OC[C@H](N)C(=O)NCC(=O)NCC(O)=O YMTLKLXDFCSCNX-BYPYZUCNSA-N 0.000 description 1
SRSPTFBENMJHMR-WHFBIAKZSA-N Ser-Ser-Gly Chemical compound OC[C@H](N)C(=O)N[C@@H](CO)C(=O)NCC(O)=O SRSPTFBENMJHMR-WHFBIAKZSA-N 0.000 description 1
108010079723 Shiga Toxin Proteins 0.000 description 1
206010054184 Small intestine carcinoma Diseases 0.000 description 1
PRXRUNOAOLTIEF-ADSICKODSA-N Sorbitan trioleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](OC(=O)CCCCCCC\C=C/CCCCCCCC)[C@H]1OC[C@H](O)[C@H]1OC(=O)CCCCCCC\C=C/CCCCCCCC PRXRUNOAOLTIEF-ADSICKODSA-N 0.000 description 1
229920002472 Starch Polymers 0.000 description 1
108010090804 Streptavidin Proteins 0.000 description 1
108010055044 Tetanus Toxin Proteins 0.000 description 1
108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
108010073919 Vascular Endothelial Growth Factor D Proteins 0.000 description 1
102100038234 Vascular endothelial growth factor D Human genes 0.000 description 1
241000251539 Vertebrata <Metazoa> Species 0.000 description 1
230000002159 abnormal effect Effects 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 description 1
230000004913 activation Effects 0.000 description 1
230000000240 adjuvant effect Effects 0.000 description 1
230000002411 adverse Effects 0.000 description 1
239000000556 agonist Substances 0.000 description 1
229930013930 alkaloid Natural products 0.000 description 1
150000003797 alkaloid derivatives Chemical class 0.000 description 1
GUBGYTABKSRVRQ-ASMJPISFSA-N alpha-maltose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-ASMJPISFSA-N 0.000 description 1
AZDRQVAHHNSJOQ-UHFFFAOYSA-N alumane Chemical class [AlH3] AZDRQVAHHNSJOQ-UHFFFAOYSA-N 0.000 description 1
XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
229910052782 aluminium Inorganic materials 0.000 description 1
WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical group [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
229910021502 aluminium hydroxide Inorganic materials 0.000 description 1
235000012211 aluminium silicate Nutrition 0.000 description 1
239000003708 ampul Substances 0.000 description 1
230000000844 anti-bacterial effect Effects 0.000 description 1
230000001093 anti-cancer Effects 0.000 description 1
239000007900 aqueous suspension Substances 0.000 description 1
230000003305 autocrine Effects 0.000 description 1
235000019445 benzyl alcohol Nutrition 0.000 description 1
229960004217 benzyl alcohol Drugs 0.000 description 1
239000011230 binding agent Substances 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
230000000903 blocking effect Effects 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
230000017531 blood circulation Effects 0.000 description 1
230000037396 body weight Effects 0.000 description 1
210000005013 brain tissue Anatomy 0.000 description 1
239000007975 buffered saline Substances 0.000 description 1
244000309464 bull Species 0.000 description 1
150000001720 carbohydrates Chemical class 0.000 description 1
235000014633 carbohydrates Nutrition 0.000 description 1
239000001768 carboxy methyl cellulose Substances 0.000 description 1
239000000969 carrier Substances 0.000 description 1
230000022131 cell cycle Effects 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
125000003636 chemical group Chemical group 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
238000011097 chromatography purification Methods 0.000 description 1
230000007012 clinical effect Effects 0.000 description 1
210000001072 colon Anatomy 0.000 description 1
239000003086 colorant Substances 0.000 description 1
230000021615 conjugation Effects 0.000 description 1
238000010276 construction Methods 0.000 description 1
230000001276 controlling effect Effects 0.000 description 1
101150005152 ctb gene Proteins 0.000 description 1
239000012531 culture fluid Substances 0.000 description 1
239000012228 culture supernatant Substances 0.000 description 1
230000001086 cytosolic effect Effects 0.000 description 1
238000013461 design Methods 0.000 description 1
235000019425 dextrin Nutrition 0.000 description 1
206010012601 diabetes mellitus Diseases 0.000 description 1
235000014113 dietary fatty acids Nutrition 0.000 description 1
UVYVLBIGDKGWPX-KUAJCENISA-N digitonin Chemical compound O([C@@H]1[C@@H]([C@]2(CC[C@@H]3[C@@]4(C)C[C@@H](O)[C@H](O[C@H]5[C@@H]([C@@H](O)[C@@H](O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)CO7)O)[C@H](O)[C@@H](CO)O6)O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O7)O)[C@@H](O)[C@@H](CO)O6)O)[C@@H](CO)O5)O)C[C@@H]4CC[C@H]3[C@@H]2[C@@H]1O)C)[C@@H]1C)[C@]11CC[C@@H](C)CO1 UVYVLBIGDKGWPX-KUAJCENISA-N 0.000 description 1
UVYVLBIGDKGWPX-UHFFFAOYSA-N digitonine Natural products CC1C(C2(CCC3C4(C)CC(O)C(OC5C(C(O)C(OC6C(C(OC7C(C(O)C(O)CO7)O)C(O)C(CO)O6)OC6C(C(OC7C(C(O)C(O)C(CO)O7)O)C(O)C(CO)O6)O)C(CO)O5)O)CC4CCC3C2C2O)C)C2OC11CCC(C)CO1 UVYVLBIGDKGWPX-UHFFFAOYSA-N 0.000 description 1
239000002270 dispersing agent Substances 0.000 description 1
238000009826 distribution Methods 0.000 description 1
238000001647 drug administration Methods 0.000 description 1
239000003480 eluent Substances 0.000 description 1
238000010828 elution Methods 0.000 description 1
239000000147 enterotoxin Substances 0.000 description 1
231100000655 enterotoxin Toxicity 0.000 description 1
238000006911 enzymatic reaction Methods 0.000 description 1
210000002919 epithelial cell Anatomy 0.000 description 1
235000019325 ethyl cellulose Nutrition 0.000 description 1
229920001249 ethyl cellulose Polymers 0.000 description 1
238000001400 expression cloning Methods 0.000 description 1
239000000194 fatty acid Substances 0.000 description 1
229930195729 fatty acid Natural products 0.000 description 1
150000004665 fatty acids Chemical class 0.000 description 1
239000012530 fluid Substances 0.000 description 1
235000019264 food flavour enhancer Nutrition 0.000 description 1
235000003599 food sweetener Nutrition 0.000 description 1
238000009472 formulation Methods 0.000 description 1
239000007789 gas Substances 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
239000011521 glass Substances 0.000 description 1
RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 1
235000003969 glutathione Nutrition 0.000 description 1
229960003180 glutathione Drugs 0.000 description 1
YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 1
125000005456 glyceride group Chemical group 0.000 description 1
238000003306 harvesting Methods 0.000 description 1
230000012447 hatching Effects 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
229930186900 holotoxin Natural products 0.000 description 1
229940116978 human epidermal growth factor Drugs 0.000 description 1
235000003642 hunger Nutrition 0.000 description 1
210000002865 immune cell Anatomy 0.000 description 1
230000003053 immunization Effects 0.000 description 1
238000009169 immunotherapy Methods 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
208000015181 infectious disease Diseases 0.000 description 1
230000002458 infectious effect Effects 0.000 description 1
238000001802 infusion Methods 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
238000003780 insertion Methods 0.000 description 1
230000037431 insertion Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
229940068935 insulin-like growth factor 2 Drugs 0.000 description 1
238000010255 intramuscular injection Methods 0.000 description 1
239000007927 intramuscular injection Substances 0.000 description 1
239000003456 ion exchange resin Substances 0.000 description 1
229920003303 ion-exchange polymer Polymers 0.000 description 1
239000007951 isotonicity adjuster Substances 0.000 description 1
NLYAJNPCOHFWQQ-UHFFFAOYSA-N kaolin Chemical compound O.O.O=[Al]O[Si](=O)O[Si](=O)O[Al]=O NLYAJNPCOHFWQQ-UHFFFAOYSA-N 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
TWNIBLMWSKIRAT-VFUOTHLCSA-N levoglucosan Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@H]2CO[C@@H]1O2 TWNIBLMWSKIRAT-VFUOTHLCSA-N 0.000 description 1
239000003446 ligand Substances 0.000 description 1
150000002632 lipids Chemical class 0.000 description 1
239000002502 liposome Substances 0.000 description 1
206010025135 lupus erythematosus Diseases 0.000 description 1
ZLNQQNXFFQJAID-UHFFFAOYSA-L magnesium carbonate Chemical compound [Mg+2].[O-]C([O-])=O ZLNQQNXFFQJAID-UHFFFAOYSA-L 0.000 description 1
239000001095 magnesium carbonate Substances 0.000 description 1
229910000021 magnesium carbonate Inorganic materials 0.000 description 1
235000019359 magnesium stearate Nutrition 0.000 description 1
210000004962 mammalian cell Anatomy 0.000 description 1
239000000594 mannitol Substances 0.000 description 1
235000010355 mannitol Nutrition 0.000 description 1
239000003550 marker Substances 0.000 description 1
230000035800 maturation Effects 0.000 description 1
238000005259 measurement Methods 0.000 description 1
230000007246 mechanism Effects 0.000 description 1
208000010658 metastatic prostate carcinoma Diseases 0.000 description 1
LXCFILQKKLGQFO-UHFFFAOYSA-N methylparaben Chemical compound COC(=O)C1=CC=C(O)C=C1 LXCFILQKKLGQFO-UHFFFAOYSA-N 0.000 description 1
239000003094 microcapsule Substances 0.000 description 1
239000004005 microsphere Substances 0.000 description 1
229940031346 monovalent vaccine Drugs 0.000 description 1
GVUGOAYIVIDWIO-UFWWTJHBSA-N nepidermin Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C(C)C)C(C)C)C1=CC=C(O)C=C1 GVUGOAYIVIDWIO-UFWWTJHBSA-N 0.000 description 1
231100000252 nontoxic Toxicity 0.000 description 1
230000003000 nontoxic effect Effects 0.000 description 1
239000007764 o/w emulsion Substances 0.000 description 1
239000004006 olive oil Substances 0.000 description 1
235000008390 olive oil Nutrition 0.000 description 1
238000007911 parenteral administration Methods 0.000 description 1
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
239000010452 phosphate Substances 0.000 description 1
150000003904 phospholipids Chemical class 0.000 description 1
230000026731 phosphorylation Effects 0.000 description 1
238000006366 phosphorylation reaction Methods 0.000 description 1
230000035479 physiological effects, processes and functions Effects 0.000 description 1
239000004033 plastic Substances 0.000 description 1
229920003023 plastic Polymers 0.000 description 1
231100000614 poison Toxicity 0.000 description 1
239000002574 poison Substances 0.000 description 1
229920001983 poloxamer Polymers 0.000 description 1
229920000747 poly(lactic acid) Polymers 0.000 description 1
229920001223 polyethylene glycol Polymers 0.000 description 1
239000004626 polylactic acid Substances 0.000 description 1
239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 1
235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
229920001451 polypropylene glycol Polymers 0.000 description 1
229950008882 polysorbate Drugs 0.000 description 1
229940068968 polysorbate 80 Drugs 0.000 description 1
229920000053 polysorbate 80 Polymers 0.000 description 1
239000002243 precursor Substances 0.000 description 1
210000002307 prostate Anatomy 0.000 description 1
238000010926 purge Methods 0.000 description 1
239000012070 reactive reagent Substances 0.000 description 1
238000005215 recombination Methods 0.000 description 1
230000006798 recombination Effects 0.000 description 1
208000020615 rectal carcinoma Diseases 0.000 description 1
210000000664 rectum Anatomy 0.000 description 1
210000002345 respiratory system Anatomy 0.000 description 1
229940085605 saccharin sodium Drugs 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 description 1
230000035939 shock Effects 0.000 description 1
239000011734 sodium Substances 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
239000000661 sodium alginate Substances 0.000 description 1
235000010413 sodium alginate Nutrition 0.000 description 1
229940005550 sodium alginate Drugs 0.000 description 1
WXMKPNITSTVMEF-UHFFFAOYSA-M sodium benzoate Chemical compound [Na+].[O-]C(=O)C1=CC=CC=C1 WXMKPNITSTVMEF-UHFFFAOYSA-M 0.000 description 1
235000010234 sodium benzoate Nutrition 0.000 description 1
239000004299 sodium benzoate Substances 0.000 description 1
235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
235000010265 sodium sulphite Nutrition 0.000 description 1
238000005507 spraying Methods 0.000 description 1
239000008107 starch Substances 0.000 description 1
235000019698 starch Nutrition 0.000 description 1
210000001562 sternum Anatomy 0.000 description 1
230000000638 stimulation Effects 0.000 description 1
238000003756 stirring Methods 0.000 description 1
238000007920 subcutaneous administration Methods 0.000 description 1
239000000126 substance Substances 0.000 description 1
125000000185 sucrose group Chemical group 0.000 description 1
238000013268 sustained release Methods 0.000 description 1
239000012730 sustained-release form Substances 0.000 description 1
239000003765 sweetening agent Substances 0.000 description 1
239000006188 syrup Substances 0.000 description 1
235000020357 syrup Nutrition 0.000 description 1
230000009885 systemic effect Effects 0.000 description 1
239000000454 talc Substances 0.000 description 1
235000012222 talc Nutrition 0.000 description 1
229910052623 talc Inorganic materials 0.000 description 1
230000008685 targeting Effects 0.000 description 1
238000013518 transcription Methods 0.000 description 1
230000035897 transcription Effects 0.000 description 1
238000012546 transfer Methods 0.000 description 1
238000010023 transfer printing Methods 0.000 description 1
210000004881 tumor cell Anatomy 0.000 description 1
230000004614 tumor growth Effects 0.000 description 1
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
238000011144 upstream manufacturing Methods 0.000 description 1
210000003708 urethra Anatomy 0.000 description 1
210000001215 vagina Anatomy 0.000 description 1
206010046885 vaginal cancer Diseases 0.000 description 1
208000013139 vaginal neoplasm Diseases 0.000 description 1
239000007762 w/o emulsion Substances 0.000 description 1
239000008215 water for injection Substances 0.000 description 1
239000000080 wetting agent Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/485—Epidermal growth factor [EGF], i.e. urogastrone
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/0005—Vertebrate antigens
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/0005—Vertebrate antigens
- A61K39/0011—Cancer antigens
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/28—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Vibrionaceae (F)
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4748—Tumour specific antigens; Tumour rejection antigen precursors [TRAP], e.g. MAGE
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/4753—Hepatocyte growth factor; Scatter factor; Tumor cytotoxic factor II
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/48—Nerve growth factor [NGF]
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/495—Transforming growth factor [TGF]
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/50—Fibroblast growth factor [FGF]
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/65—Insulin-like growth factors, i.e. somatomedins, e.g. IGF-1, IGF-2
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/71—Receptors; Cell surface antigens; Cell surface determinants for growth factors; for growth regulators
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/64—Medicinal preparations containing antigens or antibodies characterised by the architecture of the carrier-antigen complex, e.g. repetition of carrier-antigen units
- A61K2039/645—Dendrimers; Multiple antigen peptides
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/70—Multivalent vaccine
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/582—Recycling of unreacted starting or intermediate materials

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
Gastroenterology & Hepatology (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Toxicology (AREA)
Immunology (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Animal Behavior & Ethology (AREA)
Pharmacology & Pharmacy (AREA)
Microbiology (AREA)
Wood Science & Technology (AREA)
Chemical Kinetics & Catalysis (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Chemical & Material Sciences (AREA)
Biomedical Technology (AREA)
Mycology (AREA)
Epidemiology (AREA)
General Engineering & Computer Science (AREA)
Biotechnology (AREA)
Oncology (AREA)
Diabetes (AREA)
Endocrinology (AREA)
Cell Biology (AREA)
Communicable Diseases (AREA)
Peptides Or Proteins (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

CN201280067891.1A 2011-11-23 2012-11-21 重组蛋白及其治疗用途 Pending CN104066447A (zh)

Priority Applications (2)

Application Number	Priority Date	Filing Date	Title
CN201810569310.3A CN108864261A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途
CN201810569766.XA CN108864291A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途

Applications Claiming Priority (5)

Application Number	Priority Date	Filing Date	Title
US201161563128P	2011-11-23	2011-11-23
US61/563,128		2011-11-23
US201261654401P	2012-06-01	2012-06-01
US61/654,401		2012-06-01
PCT/IB2012/002876 WO2013076580A2 (en)	2011-11-23	2012-11-21	Recombinant proteins and their therapeutic uses

Related Child Applications (2)

Application Number	Title	Priority Date	Filing Date
CN201810569310.3A Division CN108864261A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途
CN201810569766.XA Division CN108864291A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途

Publications (1)

Publication Number	Publication Date
CN104066447A true CN104066447A (zh)	2014-09-24

Family

ID=47716105

Family Applications (3)

Application Number	Title	Priority Date	Filing Date
CN201810569766.XA Pending CN108864291A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途
CN201280067891.1A Pending CN104066447A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途
CN201810569310.3A Pending CN108864261A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途

Family Applications Before (1)

Application Number	Title	Priority Date	Filing Date
CN201810569766.XA Pending CN108864291A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途

Family Applications After (1)

Application Number	Title	Priority Date	Filing Date
CN201810569310.3A Pending CN108864261A (zh)	2011-11-23	2012-11-21	重组蛋白及其治疗用途

Country Status (22)

Country	Link
US (5)	US9902760B2 (sr)
EP (2)	EP2782598B1 (sr)
JP (4)	JP6121436B2 (sr)
KR (2)	KR102274211B1 (sr)
CN (3)	CN108864291A (sr)
AU (3)	AU2012342117B2 (sr)
BR (1)	BR112014012460B1 (sr)
CA (1)	CA2856255C (sr)
DK (1)	DK2782598T3 (sr)
ES (1)	ES2812564T3 (sr)
HR (1)	HRP20201282T1 (sr)
HU (1)	HUE050438T2 (sr)
IL (2)	IL232645B (sr)
LT (1)	LT2782598T (sr)
MX (2)	MX354902B (sr)
MY (2)	MY188083A (sr)
PL (1)	PL2782598T3 (sr)
PT (1)	PT2782598T (sr)
RS (1)	RS60782B1 (sr)
RU (2)	RU2650574C2 (sr)
SI (1)	SI2782598T1 (sr)
WO (1)	WO2013076580A2 (sr)

Cited By (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN107880133A (zh) *	2017-11-04	2018-04-06	海南大学	促皮质素与胰岛素样生长因子1融合蛋白及其制备方法
CN107949401A (zh) *	2015-05-12	2018-04-20	拜奥文斯瑞有限公司	联合施用酪氨酸激酶抑制剂来抑制表皮生长因子/表皮生长因子受体途径的方法及组合物
WO2019179361A1 (zh) *	2018-03-21	2019-09-26	傅惠芳	改善括约肌闭锁不全的组合物及其医药组成物与用途
CN111246878A (zh) *	2017-07-18	2020-06-05	因斯瑞拜奥有限公司	合成蛋白及其治疗用途
CN112552412A (zh) *	2019-12-05	2021-03-26	屈向东	一种包含TGF-β抑制剂、VEGF抑制剂和抗PDL1抗体的三功能融合蛋白
CN113735980A (zh) *	2021-08-23	2021-12-03	中国医学科学院北京协和医院	一种自融合串联蛋白修饰方法及其应用
CN114269792A (zh) *	2019-06-25	2022-04-01	因斯瑞拜奥有限公司	稳定的嵌合合成蛋白及其治疗用途

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN108864291A (zh) *	2011-11-23	2018-11-23	拜奥文斯瑞有限公司	重组蛋白及其治疗用途
US20190358320A1 (en) *	2015-05-12	2019-11-28	In3Bio Ltd.	Methods and compositions for inhibition of egf/egfr pathway in combination with tyrosine kinase inhibitors
US20210393768A1 (en) *	2018-08-27	2021-12-23	University Of Virginia Patent Foundation	Compositions and methods for preventing and treating virus infection
WO2021090069A1 (en)	2019-11-07	2021-05-14	In3Bio Ltd.	Methods and compositions for use of growth factor antibodies in combination with non-tyrosine targeting kinase inhibitors
WO2021195327A1 (en) *	2020-03-25	2021-09-30	The Regents Of The University Of Colorado, A Body Corporate	Bivalent egf fusion toxins

Citations (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN1142973A (zh) *	1993-12-09	1997-02-19	分子免疫中心	具有抗肿瘤活性的疫苗组合物及其在恶性疾病治疗方面的应用
CN101595219A (zh) *	2006-11-13	2009-12-02	阿特纳赞塔里斯有限公司	作为编码抗原和蛋白毒素的核苷酸序列的载体的微生物，其制备方法和用途

Family Cites Families (43)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US3238190A (en)	1963-10-23	1966-03-01	Madaus & Co K G Fa Dr	Aescin recovery
SE8205892D0 (sv)	1982-10-18	1982-10-18	Bror Morein	Immunogent membranproteinkomplex, sett for framstellning och anvendning derav som immunstimulerande medel och sasom vaccin
US5057540A (en)	1987-05-29	1991-10-15	Cambridge Biotech Corporation	Saponin adjuvant
CA1331443C (en)	1987-05-29	1994-08-16	Charlotte A. Kensil	Saponin adjuvant
CA2261433A1 (en) *	1993-12-09	1995-06-10	Belinda Sanchez Ramirez	Composition comprising autologous epidermal growth factor
GB9326253D0 (en)	1993-12-23	1994-02-23	Smithkline Beecham Biolog	Vaccines
AUPM873294A0 (en)	1994-10-12	1994-11-03	Csl Limited	Saponin preparations and use thereof in iscoms
UA56132C2 (uk)	1995-04-25	2003-05-15	Смітклайн Бічем Байолоджікалс С.А.	Композиція вакцини (варіанти), спосіб стабілізації qs21 відносно гідролізу (варіанти), спосіб приготування композиції вакцини
JPH10147952A (ja)	1996-11-18	1998-06-02	Komatsu Ltd	ブルドーザのドージング装置
EP2050465B1 (en)	1997-08-29	2014-06-11	Antigenics Inc.	Compositions comprising the adjuvant QS-21 and polysorbate or cyclodextrin as excipient
CN1294517A (zh) *	1997-11-14	2001-05-09	欧洲细胞技术有限公司	具有合成可变区和修饰特异性的免疫球蛋白分子
US6492325B1 (en) *	1998-05-22	2002-12-10	Boys Town National Research Hospital	Use of α1β1 integrin receptor inhibitors and TGF-β1 inhibitors in the treatment of kidney disease
CZ303515B6 (cs)	1999-04-19	2012-11-07	Smithkline Beecham Biologicals S. A.	Adjuvantní prostredek
US7078486B2 (en) *	1999-12-10	2006-07-18	Spectral Diagnostics, Inc.	Single-chain polypeptides comprising troponin I and troponin C
AU2001249372A1 (en) *	2000-03-23	2001-10-03	Greenville Hospital System	Bi-functional cancer treatment agents
CU22999A1 (es)	2001-12-04	2004-10-12	Centro Inmunologia Molecular	Método de tratamiento de enfermedades malignas e infecciosas crónicas
CA2447585A1 (en) *	2001-05-14	2003-01-23	Duotol Ab	Methods for promoting antigen presentation and modulating immune responses using cholera toxin and its b subunit
IL159225A0 (en) *	2001-06-13	2004-06-01	Genmab As	Human monoclonal antibodies to epidermal growth factor receptor (egfr)
US6833441B2 (en) *	2001-08-01	2004-12-21	Abmaxis, Inc.	Compositions and methods for generating chimeric heteromultimers
AU2002323236A1 (en)	2001-08-17	2003-03-03	Gerlad Elfenbein	In situ immunization
US7332585B2 (en) *	2002-04-05	2008-02-19	The Regents Of The California University	Bispecific single chain Fv antibody molecules and methods of use thereof
JP2005528107A (ja) *	2002-05-31	2005-09-22	シェジェンピーティーワイリミテッド	膜転位置配列由来の自己合体または自己凝集キメラタンパク質
AU2003900481A0 (en) *	2003-02-05	2003-02-20	Queensland University Of Technology	Synthetic modulators of cell migration and growth
US8207314B2 (en) *	2003-05-16	2012-06-26	Sanofi Pasteur Limited	Tumor antigens for prevention and/or treatment of cancer
US7601341B2 (en) *	2003-06-05	2009-10-13	Research Development Foundation	Vascular endothelial growth factor fusion constructs used to inhibit osteoclastogenesis
JP4623625B2 (ja) *	2003-07-24	2011-02-02	株式会社AMBiS	ヘテロ型５量体組換えワクチン
US7320795B2 (en) *	2003-07-30	2008-01-22	Vaccine Research Institute Of San Diego	Rodent hepatitis B virus core proteins as vaccine platforms and methods of use thereof
WO2007086879A2 (en) *	2005-02-11	2007-08-02	University Of Southern California	Method of expressing proteins with disulfide bridges
FR2882654B1 (fr) *	2005-03-01	2007-04-27	Servier Lab	Utilisation de derives de la diosmetine pour le traitement et la prevention des pathologies thrombotiques
CN1686562A (zh) *	2005-03-31	2005-10-26	南京大学	一种转铁蛋白与生物还原剂的结合物及其制备方法
KR20080100353A (ko) *	2006-02-01	2008-11-17	더 존스 홉킨스 유니버시티	신생물성 또는 감염성 질환의 면역예방 또는 면역요법용 폴리펩티드-핵산 접합체
ATE473758T1 (de) *	2006-04-13	2010-07-15	Bio Life Science Forschungs & Entwicklungsgesellschaft Mbh	Her-2/neu multipeptidimpfstoff
ES2377579T3 (es)	2006-06-02	2012-03-29	Regeneron Pharmaceuticals, Inc.	Anticuerpos de alta afinidad contra el receptor de IL-6 humano
EP2044246A4 (en)	2006-07-06	2009-12-16	Molecular Logix Inc	LIGAND DRUG DISCOVERY SYSTEM DOMINANT NEGATIVE
CA2661634C (en) *	2006-09-06	2017-03-28	The Regents Of The University Of California	Selectively targeted antimicrobial peptides and the use thereof
CN1995064A (zh) *	2006-12-20	2007-07-11	李欣越	增强生物活性的长效重组人红细胞生长因子融合蛋白及方法
MX2009008140A (es) *	2007-02-02	2009-10-26	Baylor Res Inst	Vacunas a base de antigeno dirigido a dcir expresado en celulas que presentan antigeno.
AU2008214077B2 (en) *	2007-02-02	2012-12-13	Baylor Research Institute	Multivariable antigens complexed with targeting humanized monoclonal antibody
EP2050764A1 (en)	2007-10-15	2009-04-22	sanofi-aventis	Novel polyvalent bispecific antibody format and uses thereof
KR101224468B1 (ko)	2009-05-20	2013-01-23	주식회사 파멥신	신규한 형태의 이중표적항체 및 그 용도
JP2011187653A (ja)	2010-03-08	2011-09-22	Olympus Corp	防水機器
JP6167040B2 (ja)	2010-11-05	2017-07-19	ザイムワークス，インコーポレイテッド	Ｆｃドメイン中に突然変異を有する、安定したヘテロ二量体抗体の設計
CN108864291A (zh) *	2011-11-23	2018-11-23	拜奥文斯瑞有限公司	重组蛋白及其治疗用途

2012
- 2012-11-21 CN CN201810569766.XA patent/CN108864291A/zh active Pending
- 2012-11-21 ES ES12824705T patent/ES2812564T3/es active Active
- 2012-11-21 KR KR1020197027075A patent/KR102274211B1/ko active Active
- 2012-11-21 KR KR1020147016995A patent/KR102024066B1/ko active Active
- 2012-11-21 BR BR112014012460-4A patent/BR112014012460B1/pt active IP Right Grant
- 2012-11-21 RU RU2014124923A patent/RU2650574C2/ru active
- 2012-11-21 RS RS20200986A patent/RS60782B1/sr unknown
- 2012-11-21 CA CA2856255A patent/CA2856255C/en active Active
- 2012-11-21 SI SI201231830T patent/SI2782598T1/sl unknown
- 2012-11-21 MX MX2014006232A patent/MX354902B/es active IP Right Grant
- 2012-11-21 HR HRP20201282TT patent/HRP20201282T1/hr unknown
- 2012-11-21 MX MX2018003596A patent/MX381185B/es unknown
- 2012-11-21 LT LTEP12824705.3T patent/LT2782598T/lt unknown
- 2012-11-21 DK DK12824705.3T patent/DK2782598T3/da active
- 2012-11-21 PL PL12824705T patent/PL2782598T3/pl unknown
- 2012-11-21 EP EP12824705.3A patent/EP2782598B1/en active Active
- 2012-11-21 JP JP2014542952A patent/JP6121436B2/ja active Active
- 2012-11-21 MY MYPI2018000286A patent/MY188083A/en unknown
- 2012-11-21 AU AU2012342117A patent/AU2012342117B2/en active Active
- 2012-11-21 EP EP20170470.7A patent/EP3744343A1/en not_active Withdrawn
- 2012-11-21 CN CN201280067891.1A patent/CN104066447A/zh active Pending
- 2012-11-21 CN CN201810569310.3A patent/CN108864261A/zh active Pending
- 2012-11-21 US US13/813,844 patent/US9902760B2/en active Active
- 2012-11-21 MY MYPI2014701320A patent/MY184576A/en unknown
- 2012-11-21 WO PCT/IB2012/002876 patent/WO2013076580A2/en active Application Filing
- 2012-11-21 HU HUE12824705A patent/HUE050438T2/hu unknown
- 2012-11-21 PT PT128247053T patent/PT2782598T/pt unknown
2014
- 2014-05-15 IL IL232645A patent/IL232645B/en active IP Right Grant
2016
- 2016-01-15 US US14/996,553 patent/US20160207972A1/en not_active Abandoned
2017
- 2017-03-29 JP JP2017064763A patent/JP6570081B2/ja not_active Expired - Fee Related
- 2017-11-16 US US15/814,723 patent/US11198716B2/en active Active
- 2017-11-30 AU AU2017268634A patent/AU2017268634B2/en not_active Ceased
2018
- 2018-03-09 RU RU2018108421A patent/RU2766595C2/ru active
2019
- 2019-04-04 JP JP2019072235A patent/JP6953467B2/ja active Active
2020
- 2020-02-21 AU AU2020201297A patent/AU2020201297B2/en not_active Ceased
- 2020-12-22 IL IL279676A patent/IL279676A/en unknown
2021
- 2021-09-29 JP JP2021159307A patent/JP7470669B2/ja active Active
- 2021-11-08 US US17/521,121 patent/US12030920B2/en active Active
2024
- 2024-07-02 US US18/761,743 patent/US20250066439A1/en active Pending

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN1142973A (zh) *	1993-12-09	1997-02-19	分子免疫中心	具有抗肿瘤活性的疫苗组合物及其在恶性疾病治疗方面的应用
CN101595219A (zh) *	2006-11-13	2009-12-02	阿特纳赞塔里斯有限公司	作为编码抗原和蛋白毒素的核苷酸序列的载体的微生物，其制备方法和用途

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
MICHAEL LEBENS ET AL: "a mucosally administered recombinant fusion protein vaccine against schistosomiasis protecting against immunopathology and infection", 《VACCINE》 *
居乃琥: "《酶工程手册》", 31 August 2011 *

Cited By (10)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN107949401A (zh) *	2015-05-12	2018-04-20	拜奥文斯瑞有限公司	联合施用酪氨酸激酶抑制剂来抑制表皮生长因子/表皮生长因子受体途径的方法及组合物
US12258389B2 (en)	2015-05-12	2025-03-25	In3Bio Ltd.	Methods and compositions for inhibition of EGF/EGFR pathway in combination with tyrosine kinase inhibitors
CN111246878A (zh) *	2017-07-18	2020-06-05	因斯瑞拜奥有限公司	合成蛋白及其治疗用途
US12134662B2 (en)	2017-07-18	2024-11-05	In3Bio Ltd.	Synthetic proteins and therapeutic uses thereof
CN107880133A (zh) *	2017-11-04	2018-04-06	海南大学	促皮质素与胰岛素样生长因子1融合蛋白及其制备方法
WO2019179361A1 (zh) *	2018-03-21	2019-09-26	傅惠芳	改善括约肌闭锁不全的组合物及其医药组成物与用途
CN114269792A (zh) *	2019-06-25	2022-04-01	因斯瑞拜奥有限公司	稳定的嵌合合成蛋白及其治疗用途
CN112552412A (zh) *	2019-12-05	2021-03-26	屈向东	一种包含TGF-β抑制剂、VEGF抑制剂和抗PDL1抗体的三功能融合蛋白
CN112552412B (zh) *	2019-12-05	2023-08-18	启愈生物技术(上海)有限公司	一种包含TGF-β抑制剂、VEGF抑制剂和抗PDL1抗体的三功能融合蛋白
CN113735980A (zh) *	2021-08-23	2021-12-03	中国医学科学院北京协和医院	一种自融合串联蛋白修饰方法及其应用

Also Published As

Publication number	Publication date
US12030920B2 (en)	2024-07-09
US20180162917A1 (en)	2018-06-14
WO2013076580A3 (en)	2013-08-22
US11198716B2 (en)	2021-12-14
AU2020201297B2 (en)	2022-03-10
DK2782598T3 (da)	2020-08-10
ES2812564T3 (es)	2021-03-17
PT2782598T (pt)	2020-09-02
EP2782598B1 (en)	2020-05-27
BR112014012460A2 (pt)	2017-06-06
AU2012342117B2 (en)	2017-08-31
PL2782598T3 (pl)	2021-03-08
EP2782598A2 (en)	2014-10-01
HUE050438T2 (hu)	2020-12-28
US20250066439A1 (en)	2025-02-27
CA2856255C (en)	2021-06-22
US20220153798A1 (en)	2022-05-19
IL232645B (en)	2021-01-31
MX2014006232A (es)	2015-02-10
RS60782B1 (sr)	2020-10-30
IL232645A0 (en)	2014-06-30
JP6121436B2 (ja)	2017-04-26
MX354902B (es)	2018-03-23
AU2017268634B2 (en)	2019-11-21
RU2018108421A3 (sr)	2021-06-04
JP2017137339A (ja)	2017-08-10
HRP20201282T1 (hr)	2020-11-13
SI2782598T1 (sl)	2020-12-31
CN108864291A (zh)	2018-11-23
LT2782598T (lt)	2020-07-27
CA2856255A1 (en)	2013-05-30
RU2014124923A (ru)	2015-12-27
MX381185B (es)	2025-03-12
JP6570081B2 (ja)	2019-09-04
EP3744343A1 (en)	2020-12-02
AU2020201297A1 (en)	2020-03-12
WO2013076580A2 (en)	2013-05-30
RU2650574C2 (ru)	2018-04-17
KR102024066B1 (ko)	2019-09-24
MY188083A (en)	2021-11-16
US20140248302A1 (en)	2014-09-04
JP2022023081A (ja)	2022-02-07
IL279676A (en)	2021-03-01
AU2012342117A1 (en)	2013-05-30
AU2012342117A8 (en)	2014-07-03
US20160207972A1 (en)	2016-07-21
JP2014534258A (ja)	2014-12-18
JP7470669B2 (ja)	2024-04-18
JP2019146576A (ja)	2019-09-05
AU2017268634A1 (en)	2017-12-21
RU2766595C2 (ru)	2022-03-15
KR20190112161A (ko)	2019-10-02
BR112014012460B1 (pt)	2021-01-12
KR20140108235A (ko)	2014-09-05
US9902760B2 (en)	2018-02-27
CN108864261A (zh)	2018-11-23
JP6953467B2 (ja)	2021-10-27
RU2018108421A (ru)	2019-02-25
KR102274211B1 (ko)	2021-07-09
MY184576A (en)	2021-04-06

Publication	Publication Date	Title
US12030920B2 (en)	2024-07-09	Recombinant proteins and their therapeutic uses
US12134662B2 (en)	2024-11-05	Synthetic proteins and therapeutic uses thereof
HK40041518A (en)	2021-08-20	Recombinant proteins and their therapeutic uses
HK1197890B (en)	2021-03-19	Recombinant proteins and their therapeutic uses
HK1197890A (en)	2015-02-27	Recombinant proteins and their therapeutic uses
US20220305105A1 (en)	2022-09-29	Stabilized chimeric synthetic proteins and therapeutic uses thereof

Legal Events

Date	Code	Title	Description
2014-09-24	C06	Publication
2014-09-24	PB01	Publication
2014-12-17	C10	Entry into substantive examination
2014-12-17	SE01	Entry into force of request for substantive examination
2018-11-16	RJ01	Rejection of invention patent application after publication
2018-11-16	RJ01	Rejection of invention patent application after publication	Application publication date: 20140924